Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Natalie Saldou"'
Autor:
Natalie Saldou, Ling Xia, Anita Huber, Earl R. Shelton, Robert Stephen Wilhelm, Kurt Jarnagin, Cheng Su, Ondine Harris Callan, Robert Alvarez, Rena Obernolte, Bin Li, Preston A. Baecker
Publikováno v:
Cellular Signalling. 10:427-440
Four cyclic-nucleotide phosphodiesterase (PDE) genes belonging to the PDE4 family (PDE4A, 4B, 4C and 4D) have been identified. All four isogenes, including several deletions and alterations of the amino, carboxyl and central catalytic domains, were e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::54ad9fe07b33f0b68d86157d29bfeb79
https://doi.org/10.1016/s0898-6568(97)00169-1
https://doi.org/10.1016/s0898-6568(97)00169-1
Autor:
Jodi Fausnaugh, Natalie Saldou, Hardy Chan, Daryl K. Eggers, Eric Osen, Ken Straub, Jack Lile, Frank H. Collins, Joan Chow, Leo Gu, Raymond R. Townsend, Kurt Jarnagin, Hi-Shi Chaing, Binh T. Nguyen, Jim W. Barnett, Lisa Erdos
Publikováno v:
Journal of Neurochemistry. 57:1052-1061
Recombinant human nerve growth factor (rhNGF) secreted by insect cells was purified by ion-exchange and reversed-phase chromatography to near homogeneity. The N-terminus of the secreted molecule was analogous to that of mouse salivary gland NGF. In i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ce9988524eb6a1dd21ac2d07e6e4093
https://doi.org/10.1111/j.1471-4159.1991.tb08256.x
https://doi.org/10.1111/j.1471-4159.1991.tb08256.x
Autor:
Zhengyu Yuan, Natalie Saldou, Rena Obernolte, Preston A. Baecker, James Ratzliff, Bin Li, Earl R. Shelton, Eric Osen, Kurt Jarnagin
Publikováno v:
Cell biochemistry and biophysics. 28(2-3)
Individual isozymes of family four cyclic-nucleotide phosphodiesterases (PDE-4s) were characterized and compared in order to advance our understanding of how PDE-4s regulate cAMP levels in cells. Full-length and shorter clones containing various func
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bcd67b84a8f4ceca488b47ae0d6ab38
https://pubmed.ncbi.nlm.nih.gov/9515166
https://pubmed.ncbi.nlm.nih.gov/9515166
Autor:
Natalie Saldou, Regina Leung, David C. Swinney, On-Yee So, Kurt Jarnagin, Liliana E. Scarafia, David L. Sloane
Publikováno v:
Gene. 161(2)
Lanosterol 14α-demethylase (LDM) is a cytochrome P-450 enzyme in the biosynthetic pathway of cholesterol. As such, it represents a target for cholesterol-lowering drugs. Rat LDM (rLDM) has been purified from the livers of rats treated with cholestyr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::35bf08df2efad5027773b9e97e7be84d
https://pubmed.ncbi.nlm.nih.gov/7665087
https://pubmed.ncbi.nlm.nih.gov/7665087